Thin Filament Regulation in Development

2002 ◽  
pp. 329-377 ◽  
Author(s):  
Page Anderson
Keyword(s):  
Thin Filament ◽  
Thin Filament Regulation

scholarly journals Cardiac thin filament regulation and the Frank–Starling mechanism

2014 ◽  
Vol 64 (4) ◽  
pp. 221-232 ◽  
Author(s):  
Fuyu Kobirumaki-Shimozawa ◽  
Takahiro Inoue ◽  
Seine A. Shintani ◽  
Kotaro Oyama ◽  
Takako Terui ◽  
...  
Keyword(s):  
Thin Filament ◽  
Thin Filament Regulation

scholarly journals Thin Filament Regulation of Relaxation in 3D Multi-Sarcomere Geometry

2009 ◽  
Vol 96 (3) ◽  
pp. 201a ◽  
Author(s):  
Srboljub M. Mijailovich ◽  
Oliver Kayser-Herald ◽  
Richard L. Moss ◽  
Michael A. Geeves
Keyword(s):  
Thin Filament ◽  
Thin Filament Regulation

scholarly journals Mutations in Actin Subdomain 3 That Impair Thin Filament Regulation by Troponin and Tropomyosin

1999 ◽  
Vol 274 (32) ◽  
pp. 22191-22196 ◽  
Author(s):  
Vicci L. Korman ◽  
Larry S. Tobacman
Keyword(s):  
Thin Filament ◽  
Thin Filament Regulation

scholarly journals Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres

2007 ◽  
Vol 579 (2) ◽  
pp. 313-326 ◽  
Author(s):  
Alicia Moreno-Gonzalez ◽  
Todd E. Gillis ◽  
Anthony J. Rivera ◽  
P. Bryant Chase ◽  
Donald A. Martyn ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Rabbit Skeletal Muscle ◽  
Muscle Fibres ◽  
Thin Filament Regulation ◽  
Skeletal Muscle Fibres

scholarly journals Phosphorylated HSP27 modulates the association of phosphorylated caldesmon with tropomyosin in colonic smooth muscle

2006 ◽  
Vol 291 (4) ◽  
pp. G630-G639 ◽  
Author(s):  
Sita Somara ◽  
Khalil N. Bitar
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Thin Filament ◽  
Muscle Cells ◽  
Smooth Muscle Contraction ◽  
Contractile Proteins ◽  
Concomitant Increase ◽  
Thin Filament Regulation ◽  
Hsp 27 ◽  
Actomyosin Interaction

Thin-filament regulation of smooth muscle contraction involves phosphorylation, association, and dissociation of contractile proteins in response to agonist stimulation. Phosphorylation of caldesmon weakens its association with actin leading to actomyosin interaction and contraction. Present data from colonic smooth muscle cells indicate that acetylcholine induced a significant association of caldesmon with PKCα and sustained phosphorylation of caldesmon at ser789. Furthermore, acetylcholine induced significant and sustained increase in the association of phospho-caldesmon with heat-shock protein (HSP)27 with concomitant increase in the dissociation of phospho-caldesmon from tropomyosin. At the thin filament level, HSP27 plays a crucial role in acetylcholine-induced association of contractile proteins. Present data from colonic smooth muscle cells transfected with non-phospho-HSP27 mutant cDNA indicate that the absence of phospho-HSP27 inhibits acetylcholine-induced caldesmon phosphorylation. Our results further indicate that the presence of phospho-HSP27 significantly enhances acetylcholine-induced sustained association of phospho-caldesmon with HSP27 with a concomitant increase in acetylcholine-induced dissociation of phospho-caldesmon from tropomyosin. We thus propose a model whereby upon acetylcholine-induced phosphorylation of caldesmon at ser789, the association of phospho-caldesmon (ser789) with phospho-HSP27 results in an essential conformational change leading to dissociation of phospho-caldesmon from tropomyosin. This leads to the sliding of tropomyosin on actin thus exposing the myosin binding sites on actin for actomyosin interaction.

scholarly journals Role of thin-filament regulatory proteins in relaxation of colonic smooth muscle contraction

2009 ◽  
Vol 297 (5) ◽  
pp. G958-G966 ◽  
Author(s):  
Sita Somara ◽  
Robert Gilmont ◽  
Khalil N. Bitar
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Thin Filament ◽  
Smooth Muscle Contraction ◽  
Regulatory Proteins ◽  
Actin Binding ◽  
Thin Filament Regulation ◽  
Actomyosin Interaction ◽  
Regulation Of Contraction

Coordinated regulation of smooth muscle contraction and relaxation is required for colonic motility. Contraction is associated with phosphorylation of myosin light chain (MLC20) and interaction of actin with myosin. Thin-filament regulation of actomyosin interaction is modulated by two actin-binding regulatory proteins: tropomyosin (TM) and caldesmon (CaD). TM and CaD are known to play crucial role in actomyosin interaction promoting contraction. Contraction is associated with phosphorylation of the small heat shock protein HSP27, concomitant with the phosphorylation of TM and CaD. Phosphorylation of HSP27 is attributed as being the prime modulator of thin-filament regulation of contraction. Preincubation of colonic smooth muscle cells (CSMC) with the relaxant neurotransmitter vasoactive intestinal peptide (VIP) showed inhibition in phosphorylation of HSP27 (ser78). Attenuation of HSP27 phosphorylation can result in modulation of thin-filament-mediated regulation of contraction leading to relaxation; thus the role of thin-filament regulatory proteins in a relaxation milieu was investigated. Preincubation of CSMC with VIP exhibited a decrease in phosphorylation of TM and CaD. Furthermore, CSMC preincubated with VIP showed a reduced association of TM with HSP27 and with phospho-HSP27 (ser78) whereas there was reduced dissociation of TM from CaD and from phospho-CaD. We thus propose that, in addition to alteration in phosphorylation of MLC20, relaxation is associated with alterations in thin-filament-mediated regulation that results in termination of contraction.

scholarly journals Effects of Pseudo-Phosphorylation of cTnI by P21 Activated Kinase-3 (PAK3) on Structure and Kinetics of Ca2+-Induced Cardiac Thin Filament Regulation

2010 ◽  
Vol 98 (3) ◽  
pp. 148a-149a
Author(s):  
Jayant James Jayasundar ◽  
Ranganath Mamidi ◽  
Yiexin Ouyang ◽  
Murali Chandra ◽  
Wenji Dong
Keyword(s):  
Thin Filament ◽  
Thin Filament Regulation ◽  
P21 Activated Kinase ◽  
Kinetics Of
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